KTR1_YEAST
ID KTR1_YEAST Reviewed; 393 AA.
AC P27810; D6W2G0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Alpha-1,2 mannosyltransferase KTR1;
DE EC=2.4.1.-;
GN Name=KTR1; OrderedLocusNames=YOR099W; ORFNames=YOR3189W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1541391; DOI=10.1093/genetics/130.2.273;
RA Hill K., Boone C., Goebl M., Puccia R., Sdicu A.-M., Bussey H.;
RT "Yeast KRE2 defines a new gene family encoding probable secretory proteins,
RT and is required for the correct N-glycosylation of proteins.";
RL Genetics 130:273-283(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9020857; DOI=10.1042/bj3210289;
RA Romero P.A., Lussier M., Sdicu A.-M., Bussey H.;
RT "Ktr1p is an alpha-1,2-mannosyltransferase of Saccharomyces cerevisiae.
RT Comparison of the enzymic properties of soluble recombinant Ktr1p and
RT Kre2p/Mnt1p produced in Pichia pastoris.";
RL Biochem. J. 321:289-295(1997).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Mannosyltransferase that transfers a mannose residue from
CC GDP-mannose to a range of acceptors in vitro, forming an alpha-(1->2)-
CC D-mannosyl-D-mannose linkage.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 5480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62941; CAA44713.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64021.1; -; Genomic_DNA.
DR EMBL; Z75007; CAA99296.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10876.1; -; Genomic_DNA.
DR PIR; S61659; S61659.
DR RefSeq; NP_014742.1; NM_001183518.1.
DR AlphaFoldDB; P27810; -.
DR SMR; P27810; -.
DR BioGRID; 34497; 122.
DR DIP; DIP-7181N; -.
DR IntAct; P27810; 1.
DR MINT; P27810; -.
DR STRING; 4932.YOR099W; -.
DR CAZy; GT15; Glycosyltransferase Family 15.
DR iPTMnet; P27810; -.
DR MaxQB; P27810; -.
DR PaxDb; P27810; -.
DR PRIDE; P27810; -.
DR EnsemblFungi; YOR099W_mRNA; YOR099W; YOR099W.
DR GeneID; 854266; -.
DR KEGG; sce:YOR099W; -.
DR SGD; S000005625; KTR1.
DR VEuPathDB; FungiDB:YOR099W; -.
DR eggNOG; KOG4472; Eukaryota.
DR GeneTree; ENSGT00940000176287; -.
DR HOGENOM; CLU_024327_4_1_1; -.
DR InParanoid; P27810; -.
DR OMA; GYRHNPF; -.
DR BioCyc; MetaCyc:G3O-33632-MON; -.
DR BioCyc; YEAST:G3O-33632-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P27810; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P27810; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:SGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IGI:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002685; Glyco_trans_15.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31121; PTHR31121; 1.
DR Pfam; PF01793; Glyco_transf_15; 1.
DR PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Alpha-1,2 mannosyltransferase KTR1"
FT /id="PRO_0000208242"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 35..68
FT /note="Stem region"
FT /evidence="ECO:0000250"
FT REGION 69..393
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 46022 MW; F93DDF2953EA287B CRC64;
MAKIMIPASK QPVYKKLGLL LVAVFTVYVF FHGAQYARGS APSPKYSTVL SSGSGYKYSK
VELPKYTGPR EKATFVTLVR NRDLYSLAES IKSVEDRFNS KFNYDWVFLN DEEFTDEFKN
VTSALVSGTT KYGVIPKEHW SFPEWIDEEK AAQVRKEMGE KRIIYGDSIS YRHMCRFESG
FFYRHPLMDD YDWYWRVEPD IKLHCDIDYD VFKFMKDNKK KYAFAISIKE YEATIPTLWE
TTRKFMEAHP ELIHENNMLD FVSDDQGLSY NLCHFWSNFE IAALDLWRSP AYSAYFDYLD
REGGFFYERW GDAPVHSIGA ALFLDRSEIH HFGDIGYYHV PFHSCPIDTS IRLANKCDCD
PSKDFTWHSY SCTTKFYNIN KLPKPAGWQN HIG